EC Number   |
Subunits |
Reference |
|---|
    1.2.1.79 | ? |
x * 5022, calculated, x * 51000, SDS-PAGE |
288054 |
| 1.2.1.79 | ? |
x * 60000, calculated |
708907 |
| 1.2.1.79 | dimer |
2 * 50000, recombinant His-tagged enzyme, SDS-PAGE, 2 * 50985, His-tagged enzyme, sequence calculation, 2 * 50853, recombinant enzyme, mass spectrometry |
763137 |
| 1.2.1.79 | dimer |
Sp2771 monomer is composed of N-terminal cofactor binding domain, a catalytic domain and an oligomerization domain |
725838 |
| 1.2.1.79 | homodimer |
2 * 50000, SDS-PAGE |
-, 722211 |
| 1.2.1.79 | homodimer |
2 * 51600, calculated from sequence |
-, 722211 |
| 1.2.1.79 | homodimer |
gel filtration, SySSADH monomer consists of three segments - alpha/beta-fold N- and C-domains for a cofactor binding and a catalytic domain, and three antiparallel beta-strands constituting a dimerization domain |
725523 |
| 1.2.1.79 | homodimer |
the overall structure of monomeric SySSADH is reminiscent of an ALDH fold. It is made up of three segments: alpha/beta-fold N- and C-domains for a cofactor binding and a catalytic domain, respectively, and three antiparallel beta-strands constituting a dimerization domain |
-, 742844 |
| 1.2.1.79 | homotetramer |
4 * 52000, SDS-PAGE |
763015 |
| 1.2.1.79 | More |
the central parts of both cofactor binding domain and catalytic domain contain atypical alpha/beta structure. The catalytic domain consists of a seven stranded beta-sheet flanked by two alpha-helices on one side and three alpha-helices on the other side.The cofactor binding domain displays the two tandem Rossmann folds for NADP+ binding . The oligomerization domain contains three-stranded antiparallel beta-sheets protruding across the center of the dimer interface, while the NADP+ binding site is on the opposite side of the dimer interface |
743181 |
